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Volumn 13, Issue 10, 2012, Pages

Enhanced top-down characterization of histone post-translational modifications

Author keywords

histone; posttranslational modification; Saltless WCX HILIC; top down

Indexed keywords

HISTONE; ISOPROTEIN;

EID: 84866882318     PISSN: None     EISSN: 1474760X     Source Type: Journal    
DOI: 10.1186/gb-2012-13-10-R86     Document Type: Article
Times cited : (119)

References (27)
  • 1
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications.
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000, 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code.
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001, 293(5532):1074-1080.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 0029869172 scopus 로고    scopus 로고
    • Histone deacetylase: A regulator of transcription.
    • Wolffe AP. Histone deacetylase: A regulator of transcription. Science 1996, 272:371-372.
    • (1996) Science , vol.272 , pp. 371-372
    • Wolffe, A.P.1
  • 4
    • 70349592855 scopus 로고    scopus 로고
    • Histone modifications during DNA replication.
    • Falbo KB, Shen XT. Histone modifications during DNA replication. Mol Cells 2009, 28:149-154.
    • (2009) Mol Cells , vol.28 , pp. 149-154
    • Falbo, K.B.1    Shen, X.T.2
  • 5
    • 28444456705 scopus 로고    scopus 로고
    • The histone code at DNA breaks: A guide to repair?.
    • van Attikum H, Gasser SM. The histone code at DNA breaks: A guide to repair?. Nat Rev Mol Cell Biol 2005, 6:757-765.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 757-765
    • van Attikum, H.1    Gasser, S.M.2
  • 7
    • 67650403817 scopus 로고    scopus 로고
    • Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum.
    • Trelle MB, Salcedo-Amaya AM, Cohen AM, Stunnenberg HG, Jensen ON. Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum. J Proteome Res 2009, 8:3439-3450.
    • (2009) J Proteome Res , vol.8 , pp. 3439-3450
    • Trelle, M.B.1    Salcedo-Amaya, A.M.2    Cohen, A.M.3    Stunnenberg, H.G.4    Jensen, O.N.5
  • 9
    • 33646900510 scopus 로고    scopus 로고
    • The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure.
    • Mersfelder EL, Parthun MR. The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure. Nucleic Acids Res 2006, 34:2653-2662.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2653-2662
    • Mersfelder, E.L.1    Parthun, M.R.2
  • 10
    • 77953981614 scopus 로고    scopus 로고
    • Going global: novel histone modifications in the globular domain of H3.
    • Tropberger P, Schneider R. Going global: novel histone modifications in the globular domain of H3. Epigenetics 2010, 5:112-117.
    • (2010) Epigenetics , vol.5 , pp. 112-117
    • Tropberger, P.1    Schneider, R.2
  • 13
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry.
    • Pesavento JJ, Bullock CR, Leduc RD, Mizzen CA, Kelleher NL. Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry. J Biol Chem 2008, 283:14927-14937.
    • (2008) J Biol Chem , vol.283 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    Leduc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 14
    • 0030606909 scopus 로고    scopus 로고
    • Separation of acetylated core histones by hydrophilic-interaction liquid chromatography.
    • Lindner H, Sarg B, Meraner C, Helliger W. Separation of acetylated core histones by hydrophilic-interaction liquid chromatography. J Chromatog A 1996, 743:137-144.
    • (1996) J Chromatog A , vol.743 , pp. 137-144
    • Lindner, H.1    Sarg, B.2    Meraner, C.3    Helliger, W.4
  • 15
    • 0037131426 scopus 로고    scopus 로고
    • Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging.
    • Sarg B, Koutzamani E, Helliger W, Rundquist I, Lindner HH. Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging. J Biol Chem 2002, 277:39195-39201.
    • (2002) J Biol Chem , vol.277 , pp. 39195-39201
    • Sarg, B.1    Koutzamani, E.2    Helliger, W.3    Rundquist, I.4    Lindner, H.H.5
  • 16
    • 51549111791 scopus 로고    scopus 로고
    • Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) of peptides and proteins.
    • Mant CT, Hodges RS. Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) of peptides and proteins. J Sep Sci 2008, 31:2754-2773.
    • (2008) J Sep Sci , vol.31 , pp. 2754-2773
    • Mant, C.T.1    Hodges, R.S.2
  • 18
    • 33644702025 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair.
    • Zhou H, Madden BJ, Muddimanm DC, Zhang ZG. Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair. Biochemistry 2006, 45:2852-2861.
    • (2006) Biochemistry , vol.45 , pp. 2852-2861
    • Zhou, H.1    Madden, B.J.2    Muddimanm, D.C.3    Zhang, Z.G.4
  • 19
    • 71049141077 scopus 로고    scopus 로고
    • A mixed integer linear optimization framework for the identification and quantification of targeted post-translational modifications of highly modified proteins using multiplexed electron transfer dissociation tandem mass spectrometry.
    • DiMaggio PA, Young NL, Baliban RC, Garcia BA, Floudas CA. A mixed integer linear optimization framework for the identification and quantification of targeted post-translational modifications of highly modified proteins using multiplexed electron transfer dissociation tandem mass spectrometry. Mol Cell Proteomics 2009, 8:2527-2543.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2527-2543
    • DiMaggio, P.A.1    Young, N.L.2    Baliban, R.C.3    Garcia, B.A.4    Floudas, C.A.5
  • 22
    • 84878060959 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00070.
    • Peptide Atlas Dataset identifier PASS00070. , http://www.peptideatlas.org/PASS/PASS00070
  • 23
    • 84878102262 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00071.
    • Peptide Atlas Dataset identifier PASS00071. , http://www.peptideatlas.org/PASS/PASS00071
  • 24
    • 84878097120 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00072.
    • Peptide Atlas Dataset identifier PASS00072. , http://www.peptideatlas.org/PASS/PASS00072
  • 25
    • 84878070844 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00073
    • Peptide Atlas Dataset identifier PASS00073. , http://www.peptideatlas.org/PASS/PASS00073
  • 26
    • 84878070844 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00074
    • Peptide Atlas Dataset identifier PASS00074. , http://www.peptideatlas.org/PASS/PASS00074
  • 27
    • 84878070844 scopus 로고    scopus 로고
    • Peptide Atlas Dataset identifier PASS00075
    • Peptide Atlas Dataset identifier PASS00075. , http://www.peptideatlas.org/PASS/PASS00075


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.